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CATH Superfamily 3.40.30.10

Glutaredoxin

The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Glutaredoxin
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 79782: Probable protein disulfide-isomerase A6

There are 5 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Protein disulfide-isomerase. [EC: 5.3.4.1]
Catalyzes the rearrangement of -S-S- bonds in proteins.
  • Needs reducing agents or partly reduced enzyme; the reaction depends on sulfhydryl-disulfide interchange.
 1332 A0A016UT30 A0A016UT30 A0A016UVV1 A0A016UVV1 A0A023B1Z1 A0A023B1Z1 A0A024G9A0 A0A024G9A0 A0A024V8E5 A0A024V8E5
(1322 more...)
Adenylyl-sulfate reductase (glutathione). [EC: 1.8.4.9]
AMP + sulfite + glutathione disulfide = adenylyl sulfate + 2 glutathione.
  • Differs from EC 1.8.99.2, in using glutathione as the reductant.
  • Glutathione can be replaced by gamma-glutamylcysteine or dithiothreitol, but not by thioredoxin, glutaredoxin or mercaptoethanol.
  • The enzyme from Arabidopsis thaliana contains a glutaredoxin-like domain.
  • Also found in other photosynthetic eukaryotes, e.g., the Madagascar periwinkle, Catharanthus roseus and the hollow green seaweed, Enteromorpha intestinalis.
 4 B7PBW3 B7PBW3 B7PBW3 B7PBW3
Thiol oxidase. [EC: 1.8.3.2]
2 R'C(R)SH + O(2) = R'C(R)S-S(R)CR' + H(2)O(2).
  • R may be =S or =O, or a variety of other groups.
  • The enzyme is not specific for R'.
 4 G0QMR6 G0QMR6 G0QMR6 G0QMR6
Protein-disulfide reductase. [EC: 1.8.1.8]
Protein dithiol + NAD(P)(+) = protein disulfide + NAD(P)H.
  • Formerly EC 1.6.4.4.
 2 B0E8U5 B0E8U5
Dolichyl-diphosphooligosaccharide--protein glycotransferase. [EC: 2.4.99.18]
Dolichyl diphosphooligosaccharide + [protein]-L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.
  • Occurs in eukaryotes that form a glycoprotein by the transfer of a glucosyl-mannosyl-glucosamine polysaccharide to the side-chain of an L-asparagine residue in the sequence -Asn-Xaa-Ser- or -Asn-Xaa-Thr- (Xaa not Pro) in nascent polypeptide chains.
  • The basic oligosaccharide is the tetradecasaccharide Glc(3)Man(9)GlcNAc(2).
  • However, smaller oligosaccharides derived from it and oligosaccharides with additional monosaccharide units attached may be involved.
  • Man(3)GlcNAc(2) seems to be common for all of the oligosaccharides involved with the terminal N-acetylglucosamine linked to the protein L-asparagine.
  • Occurs on the cytosolic face of the endoplasmic reticulum.
  • The dolichol involved normally has 14-21 isoprenoid units with two trans double-bonds at the omega end, and the rest of the double-bonds in cis form.
  • Formerly EC 2.4.1.119.
 2 L1LC14 L1LC14
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